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Molecular Details of Urease Inhibition by Boric Acid: Insights into the Catalytic Mechanism

Benini, Stefano, Rypniewski, Wojciech R., Wilson, Keith S., Mangani, Stefano, Ciurli, Stefano·2004·Journal of the American Chemical Society

Abstract

The structure of the complex of urease, a Ni-containing metalloenzyme, with boric acid was determined at 2.10 A resolution. The complex shows the unprecedented binding mode of the competitive inhibitor to the dinuclear metal center, with the B(OH)3 molecule bridging the Ni ions and leaving in place the bridging hydroxide. Boric acid can be considered a substrate analogue of urea, and the structure supports the proposal that the Ni-bridging hydroxide acts as the nucleophile in the enzymatic process of urea hydrolysis.

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Metadata

Authors
Benini, S., Rypniewski, W. R., Wilson, K. S., Mangani, S., & Ciurli, S.
Venue
Journal of the American Chemical Society
Published
2004-03-01
Volume
126
Issue
12
Pages
3714-3715
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2000312207
Cited by
172
References
0
FWCI
3.96
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Molecular Details of Urease Inhibition by Boric Acid: Insights into the Catalytic Mechanism. https://app.cochat.ai/papers/10.1021/ja049618p
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Benini, S., Rypniewski, W. R., Wilson, K. S., Mangani, S., & Ciurli, S. (2004). Molecular Details of Urease Inhibition by Boric Acid: Insights into the Catalytic Mechanism. Journal of the American Chemical Society. https://doi.org/10.1021/ja049618p

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.